S47A2_RABIT
ID S47A2_RABIT Reviewed; 601 AA.
AC A7KAU3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Multidrug and toxin extrusion protein 2;
DE Short=MATE-2;
DE AltName: Full=Solute carrier family 47 member 2;
GN Name=SLC47A2; Synonyms=MATE2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND FUNCTION.
RX PubMed=17442726; DOI=10.1152/ajprenal.00102.2007;
RA Zhang X., Cherrington N.J., Wright S.H.;
RT "Molecular identification and functional characterization of rabbit MATE1
RT and MATE2-K.";
RL Am. J. Physiol. 293:F360-F370(2007).
CC -!- FUNCTION: Solute transporter for tetraethylammonium (TEA), 1-methyl-4-
CC phenylpyridinium (MPP), cimetidine, N-methylnicotinamide, metformin,
CC creatinine, guanidine, procainamide, topotecan, estrone sulfate,
CC acyclovir, and ganciclovir. Responsible for the secretion of cationic
CC drugs across the brush border membranes. {ECO:0000269|PubMed:17442726}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:17442726};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Apical cell membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Note=Predominantly found in the apical
CC membrane of RPT cells.
CC -!- TISSUE SPECIFICITY: Expressed in renal cortical tissues.
CC {ECO:0000269|PubMed:17442726}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-30 is the initiator.
CC {ECO:0000305}.
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DR EMBL; EF121852; ABP96920.1; -; mRNA.
DR RefSeq; NP_001103290.2; NM_001109820.2.
DR AlphaFoldDB; A7KAU3; -.
DR SMR; A7KAU3; -.
DR STRING; 9986.ENSOCUP00000010244; -.
DR GeneID; 100125996; -.
DR KEGG; ocu:100125996; -.
DR CTD; 146802; -.
DR eggNOG; KOG1347; Eukaryota.
DR InParanoid; A7KAU3; -.
DR OrthoDB; 743037at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR CDD; cd13132; MATE_eukaryotic; 1.
DR InterPro; IPR045069; MATE_euk.
DR InterPro; IPR002528; MATE_fam.
DR Pfam; PF01554; MatE; 2.
DR TIGRFAMs; TIGR00797; matE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..601
FT /note="Multidrug and toxin extrusion protein 2"
FT /id="PRO_0000311954"
FT TOPO_DOM 1..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..95
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..601
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 601 AA; 64175 MW; 571A84BF28E95F02 CRC64;
MNTAFAGFDE NRAGRRAPGC TGRPAFGLGM DSQQDVVNLD QGGCCPALRK LLPRGFWDEA
RALFVLSGPL FLFQVLNFLT YVVGTVFCGH LGKVELASVT LGVAFVNVCG VSVGAGLSSA
CDTLMSQSFG SPNKKHVGVI LQRGSLILLL CCLPCWALFL NTQHILLLFR QDPAVSRLTQ
DYAMIFIPGL PAIFLYSLLA KYLQNQGIVW PQVLSGVVGN CVNGVANYAL VSVLNLGVRG
SAYANTISQF VQAAFLFLHI VLKKLHLETW EGWSSQCLRD WGPFLSLAIP SMLMMCVEWW
AYEIGSFLMG LLGVVDLSGQ AIIYEVATVV YMIPMGLGMA VCVRVGTALG AADTLQAKRS
AVSGLLCTAG TSLVVGTLLG LLNSQLGYIF TSDEEVIALV NQVLPIYIVF QLVEAVCCVF
GGVLRGTGKQ AFGAIVNAIM YYIVGLPLGI VLTFVVGMRI MGLWLGMLTC IFLAAVTFVV
YAVQLDWKLA AEEAQKHAGL QQQQQQQQQQ GAECTAPSPG PDKAVVSSVA TGCNPGIALT
MYSRPGCHVD FYGRPEAAPA PAAPASRLSV RQLLFRRGAA LAASVAVLMA GLLVRVLTTG
Y
